3ETJ
Crystal structure E. coli Purk in complex with Mg, ADP, and Pi
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004638 | molecular_function | phosphoribosylaminoimidazole carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0034028 | molecular_function | 5-(carboxyamino)imidazole ribonucleotide synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ADP A 400 |
| Chain | Residue |
| A | ARG80 |
| A | GLY155 |
| A | ILE156 |
| A | PHE158 |
| A | GLU161 |
| A | HIS184 |
| A | GLY187 |
| A | GLU226 |
| A | PHE228 |
| A | ASN237 |
| A | GLU238 |
| A | LYS120 |
| A | MG401 |
| A | MG402 |
| A | PI403 |
| A | HOH463 |
| A | HOH688 |
| A | HOH693 |
| A | HOH694 |
| A | HOH695 |
| A | TYR126 |
| A | ASP127 |
| A | GLY128 |
| A | GLN131 |
| A | ARG133 |
| A | GLU153 |
| A | GLN154 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | GLU226 |
| A | GLU238 |
| A | ADP400 |
| A | PI403 |
| A | HOH694 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | GLU238 |
| A | ADP400 |
| A | PI403 |
| A | HOH635 |
| A | HOH695 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PI A 403 |
| Chain | Residue |
| A | TYR126 |
| A | ASP127 |
| A | GLU226 |
| A | GLU238 |
| A | ARG242 |
| A | HIS244 |
| A | ADP400 |
| A | MG401 |
| A | MG402 |
| A | HOH473 |
| A | HOH625 |
| A | HOH635 |
| A | HOH694 |
| A | HOH696 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP B 400 |
| Chain | Residue |
| B | ARG80 |
| B | ILE118 |
| B | LYS120 |
| B | GLN131 |
| B | GLU153 |
| B | GLN154 |
| B | GLY155 |
| B | ILE156 |
| B | PHE158 |
| B | GLU161 |
| B | HIS184 |
| B | GLU226 |
| B | PHE228 |
| B | ASN237 |
| B | GLU238 |
| B | MG401 |
| B | MG402 |
| B | PI403 |
| B | HOH497 |
| B | HOH530 |
| B | HOH659 |
| B | HOH661 |
| B | HOH666 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | GLU226 |
| B | GLU238 |
| B | ADP400 |
| B | PI403 |
| B | HOH659 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | GLU238 |
| B | ADP400 |
| B | PI403 |
| B | HOH660 |
| B | HOH661 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PI B 403 |
| Chain | Residue |
| B | GLU226 |
| B | GLU238 |
| B | ARG242 |
| B | HIS244 |
| B | ADP400 |
| B | MG401 |
| B | MG402 |
| B | HOH442 |
| B | HOH660 |
| B | HOH664 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 404 |
| Chain | Residue |
| A | ARG242 |
| A | VAL243 |
| A | HIS262 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:10569930, ECO:0000269|PubMed:19053251 |
| Chain | Residue | Details |
| A | ARG80 | |
| B | GLY125 | |
| B | GLU153 | |
| B | GLU161 | |
| B | HIS184 | |
| B | ASN237 | |
| A | LYS120 | |
| A | GLY125 | |
| A | GLU153 | |
| A | GLU161 | |
| A | HIS184 | |
| A | ASN237 | |
| B | ARG80 | |
| B | LYS120 |
